The distribution and turnover of the collagen populations in the cornea, sclera and lens capsules of rabbit eyes will be analyzed. The constituent polypeptide chains from the pepsin-solubilized collagens will be identified and quantified by gel electrophoresis, and the rate of synthesis and catabolism will be measured by the incorporation of radiolabeled proline. Localization of the collagens in tissues will employ immunolabeling; attempts to prepare monoclonal antibodies are under way. The development of the mature pattern of cross-linking in the collagen will be studied with pulse-labeling and analysis of the cyanogen bromide peptides recovered from the intact tissue and the pepsin solubilized collagen.